2007
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
SKRISOVSKA, Lenka; Cyril BOURGEOIS; Richard ŠTEFL; Sushma-Nagaraja GRELLSCHEID; Liliane KISTER et al.Základní údaje
Originální název
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
Název česky
The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction
Autoři
SKRISOVSKA, Lenka; Cyril BOURGEOIS; Richard ŠTEFL; Sushma-Nagaraja GRELLSCHEID; Liliane KISTER; Philipp WENTER; David ELLIOTT; James STEVENIN a Frederic ALLAIN
Vydání
EMBO REPORTS, Nature Publishing Group, London, UK, Nature Publishing Group, London, UK, 2007, 1469-221X
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 7.450
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/07:00022207
Organizační jednotka
Přírodovědecká fakulta
UT WoS
Klíčová slova anglicky
alternative splicing; NMR; protein-nucleic acid recognition; spermatogenesis; SELEX
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 29. 6. 2008 06:06, Olga Křížová
V originále
The RBMY (RNA binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem loops capped by a C(A/U)CAA pentaloop are high affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high affinity target showed two distinct modes of RNA recognition. First, the RRM beta sheet surface binds to the RNA loop in a sequence specific fashion. Second, the beta2 beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis.
Česky
The RBMY (RNA-binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem-loops capped by a C(A/U)CAA pentaloop are high-affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high-affinity target showed two distinct modes of RNA recognition. First, the RRM beta-sheet surface binds to the RNA loop in a sequence-specific fashion. Second, the beta2-beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis.
Návaznosti
| MSM0021622413, záměr |
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